ID A0A498LEN5_LABRO Unreviewed; 1517 AA.
AC A0A498LEN5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Xylosyltransferase 2 {ECO:0000256|ARBA:ARBA00039683};
DE EC=2.4.2.26 {ECO:0000256|ARBA:ARBA00011972};
DE AltName: Full=Xylosyltransferase II {ECO:0000256|ARBA:ARBA00041721};
GN ORFNames=ROHU_012278 {ECO:0000313|EMBL:RXN06681.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN06681.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN06681.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN06681.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN06681.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-
CC L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:50192, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:12567, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132085; EC=2.4.2.26;
CC Evidence={ECO:0000256|ARBA:ARBA00001814};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004840}.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005093}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT
CC subfamily. {ECO:0000256|ARBA:ARBA00010195}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN06681.1}.
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DR EMBL; QBIY01013359; RXN06681.1; -; Genomic_DNA.
DR STRING; 84645.A0A498LEN5; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030158; F:protein xylosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00992; PDZ_signaling; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR015098; EBP50_C.
DR InterPro; IPR003406; Glyco_trans_14.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR043538; XYLT.
DR InterPro; IPR024448; XylT_C.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR46025:SF1; XYLOSYLTRANSFERASE 2; 1.
DR PANTHER; PTHR46025; XYLOSYLTRANSFERASE OXT; 1.
DR Pfam; PF02485; Branch; 1.
DR Pfam; PF09007; EBP50_C; 1.
DR Pfam; PF00595; PDZ; 2.
DR Pfam; PF00071; Ras; 2.
DR Pfam; PF12529; Xylo_C; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RXN06681.1}.
FT DOMAIN 1151..1231
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1314..1394
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 74..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1439..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1486..1517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1517 AA; 169527 MW; 2CE24743695E8047 CRC64;
MVASTRVQKL LRRYKLAIAA GLTILLIQGL VVWSLRSLEE GEAERKHRRS KLPDHNGQEQ
KLDPVAFERQ NALSGANHGQ SRQRQDQPAV TTIIRRGSRR RNKPSLKDKS LGGPEDGVAA
EKAAHYDPSS SRNFSDTRAG EMAKIHLVAP GEPGSVEGAP QVPNSDFVPK CEISGKDALS
ALHRAGSRQC RQEIANIVCQ HQAGQLMPQS LPQFCPQHVI SSAVQHADFA DADLSKVENP
VRVVFMLVVH GRAVRQLKRL LKAIYHKDHF YYIHVDKRSN YMHREVLQMA ELYPNVRATP
WRMVTIWGGA SLLKAYLRSM HDLLSMLDWK WDFFINLSAT DFPTRTNDEL VAFLSQNRDK
NFLKSHGREN ARFIKKQGLD RLFHECDNHM WRLGERTIPE GLEVSGGSDW FSLTRKFVEY
VVNSQDELVT GLKQFYTYAL LPAESFFHTV LGNSHMCDTL VDNNLRVTNW NRKLGCKCQY
KHIVDWCGCS PNDFKPSDLI RIQQLTRPTF FARKFESTVN QEAIEILDNH LYGQYPPGTV
ALKAYWESLF EQADGVSSLN DVALTAYSSF FRLGLHKPET PQSSSEACRF EPIGYPASVH
LYFYDDRFQG YLVRQEVQNV VTRSREILEV WAVPQATLQL EHNLHEFERL KHLEVGTDWD
PKERIFRNFG SVMGPLDEPV AVQKWARGPN LTATIVWIDP AHIVAASYDI SIDVEAEFTQ
YKPPLQRPLR PGVWTVRVLR LWERVAEARF LVMPLAFKGR EPLRAEDHGW VHGGPPGNVY
LEQSFQQLAN VLKLPPSEPA LQEAQKKTTL VGKPLEAWVD SSVGAFWVTG DLCSEVTSSC
STIGLCTKTS WSSLSPDPKS ELGPVKKDGR ISTSHMELMM ENTSDLEPVE QGEPAYPDSA
YGSSPVDMDT EDGDTLSSST LLLTYNEELM HKTILVGDSG VGKTSLLVQF DQGKFITGSF
SATVGIGFTV MLLGDSAVGK TCVLVRFKDG AFLGGNFIAT VGIDFRNKVV TVDNMKVKLQ
IWDTAGQERF RSVTHAYYRD AQGKYATFTD TFANLLTDFV TGVISSAWLT EIYEYAQKDV
VIMLLGNKSD MAAERVIAHE EGEKLAKEYG VPFMETSAKT GVNVELAFHA IARFDQQVTR
VMPSQTLRPR LCVLEKGENG YGFHLHGEKG KSGQFIRLVE PDSPAELAGL RAGDRLVFVN
GERVESDSHQ QVVARIRSSD GNLELIVVDV DTDQLLKKHE LKCLKEFVTE GIPVPECDDE
PEISDEMMRE DTPPPPPVPE RKGEIIPVHI PVVEKLRTSV SSETDLKLHL RPRLCVIKKG
PSGFGFNLHS EKNRPGQYIR AIDEDSPAQR SGLKPKDRLI QVNGVLVEGK QHAEVVATIK
AGGDNTSLLV VDPDTDAFFK KCRVTPSAEH LTGPLPEPVV NGDMEDKVNG NVAKEVELKD
SKLSISPSPS NASSNASLTT PPTGTPPPEA VEASIIDAIP ELNLSLQQVK ERAHQKRSNK
KAPPMDWNKK NELFSNL
//
